3LWZ
1.65 Angstrom Resolution Crystal Structure of Type II 3-Dehydroquinate Dehydratase (aroQ) from Yersinia pestis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0009423 | biological_process | chorismate biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019631 | biological_process | quinate catabolic process |
| B | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0009423 | biological_process | chorismate biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019631 | biological_process | quinate catabolic process |
| C | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| C | 0009423 | biological_process | chorismate biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019631 | biological_process | quinate catabolic process |
| D | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| D | 0009423 | biological_process | chorismate biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019631 | biological_process | quinate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME A 151 |
| Chain | Residue |
| A | ASN106 |
| A | VAL107 |
| A | HIS108 |
| A | CYS128 |
| A | GOL152 |
| D | BME151 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 152 |
| Chain | Residue |
| A | ARG114 |
| A | HIS115 |
| A | HIS116 |
| A | SER117 |
| A | SER120 |
| A | VAL126 |
| A | BME151 |
| D | HIS108 |
| A | HIS83 |
| A | GLU101 |
| A | HIS108 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 153 |
| Chain | Residue |
| A | ALA79 |
| A | HIS83 |
| A | SER105 |
| A | ARG110 |
| A | ARG114 |
| A | HOH164 |
| A | HOH305 |
| A | HOH641 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 154 |
| Chain | Residue |
| A | LEU92 |
| A | GLN96 |
| A | ILE97 |
| A | PRO98 |
| A | PHE99 |
| A | HOH157 |
| A | HOH192 |
| A | HOH302 |
| A | HOH372 |
| A | HOH625 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 155 |
| Chain | Residue |
| A | SER117 |
| A | TYR118 |
| A | ASP121 |
| D | HIS115 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 156 |
| Chain | Residue |
| A | GLU111 |
| A | HOH557 |
| A | HOH590 |
| B | ARG89 |
| B | HOH196 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME B 151 |
| Chain | Residue |
| B | ASN106 |
| B | VAL107 |
| B | HIS108 |
| B | CYS128 |
| B | GOL153 |
| C | BME151 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 152 |
| Chain | Residue |
| B | ALA79 |
| B | HIS83 |
| B | SER105 |
| B | ARG110 |
| B | ARG114 |
| B | HOH244 |
| B | HOH497 |
| B | HOH505 |
| B | HOH566 |
| B | HOH643 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 153 |
| Chain | Residue |
| B | HIS83 |
| B | GLU101 |
| B | HIS103 |
| B | HIS108 |
| B | ARG114 |
| B | HIS115 |
| B | HIS116 |
| B | SER117 |
| B | SER120 |
| B | BME151 |
| C | HIS108 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 154 |
| Chain | Residue |
| B | LEU92 |
| B | GLN96 |
| B | ILE97 |
| B | PHE99 |
| B | HOH155 |
| B | HOH515 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME C 151 |
| Chain | Residue |
| B | BME151 |
| C | ASN106 |
| C | VAL107 |
| C | VAL126 |
| C | CYS128 |
| C | GOL153 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 152 |
| Chain | Residue |
| A | HOH634 |
| C | ALA79 |
| C | HIS83 |
| C | SER105 |
| C | ARG110 |
| C | ARG114 |
| C | HOH181 |
| C | HOH187 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C 153 |
| Chain | Residue |
| C | SER120 |
| C | BME151 |
| B | HIS108 |
| C | HIS83 |
| C | GLU101 |
| C | HIS108 |
| C | ARG114 |
| C | HIS115 |
| C | HIS116 |
| C | SER117 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 154 |
| Chain | Residue |
| C | ARG89 |
| C | HIS116 |
| C | SER117 |
| C | ASP121 |
| C | HOH220 |
| C | HOH667 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME D 151 |
| Chain | Residue |
| A | BME151 |
| D | ASN106 |
| D | VAL107 |
| D | HIS108 |
| D | CYS128 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 152 |
| Chain | Residue |
| D | HIS51 |
| D | SER63 |
| D | HOH169 |
| D | HOH171 |
| D | HOH273 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 153 |
| Chain | Residue |
| D | ALA79 |
| D | HIS83 |
| D | SER105 |
| D | ARG110 |
| D | ARG114 |
| D | HOH214 |
| D | HOH338 |
| D | HOH619 |
| D | HOH642 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 154 |
| Chain | Residue |
| D | ARG89 |
| D | HIS116 |
| D | SER117 |
| D | TYR118 |
| D | ASP121 |
| D | HOH245 |
| site_id | CC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 155 |
| Chain | Residue |
| A | HIS108 |
| D | HIS83 |
| D | GLU101 |
| D | HIS108 |
| D | ARG114 |
| D | HIS115 |
| D | HIS116 |
| D | SER117 |
| D | SER120 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 156 |
| Chain | Residue |
| D | ARG110 |
| D | GLU111 |
| D | HOH601 |
| D | HOH640 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 157 |
| Chain | Residue |
| D | LEU92 |
| D | GLN96 |
| D | ILE97 |
| D | PRO98 |
| D | PHE99 |
| D | HOH160 |
| D | HOH322 |
| D | HOH655 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 158 |
| Chain | Residue |
| D | GLU39 |
| D | ALA42 |
| D | GLN43 |
| D | VAL47 |
| D | ALA48 |
| D | LEU49 |
| D | HOH550 |
Functional Information from PROSITE/UniProt
| site_id | PS01029 |
| Number of Residues | 18 |
| Details | DEHYDROQUINASE_II Dehydroquinase class II signature. LNGPNLnlLGtREpekYG |
| Chain | Residue | Details |
| A | LEU10-GLY27 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
